Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Anamorsin

Gene

CIAPIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1 (PubMed:23596212). NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit (By similarity). Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells (By similarity).UniRule annotationBy similarity1 Publication

Miscellaneous

'Ana-mors-in' means 'anti-death molecule' in Latin.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi237Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi246Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi249Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi251Iron-sulfur (2Fe-2S)UniRule annotation1
Metal bindingi274Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi277Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi285Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi288Iron-sulfur (4Fe-4S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • hemopoiesis Source: Ensembl
  • iron-sulfur cluster assembly Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB

Keywordsi

Biological processApoptosis
Ligand2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-2564830 Cytosolic iron-sulfur cluster assembly

Names & Taxonomyi

Protein namesi
Recommended name:
AnamorsinUniRule annotation
Alternative name(s):
Cytokine-induced apoptosis inhibitor 1UniRule annotation
Fe-S cluster assembly protein DRE2 homologUniRule annotation
Gene namesi
Name:CIAPIN1UniRule annotation
ORF Names:CUA001, PRO0915
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000005194.14
HGNCiHGNC:28050 CIAPIN1
MIMi608943 gene
neXtProtiNX_Q6FI81

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi57019
OpenTargetsiENSG00000005194
PharmGKBiPA134978864

Polymorphism and mutation databases

BioMutaiCIAPIN1
DMDMi57012667

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000792881 – 312AnamorsinAdd BLAST312

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei136PhosphothreonineCombined sources1
Modified residuei177PhosphoserineCombined sources1
Modified residuei182PhosphoserineCombined sources1
Modified residuei183PhosphoserineCombined sources1
Modified residuei215PhosphoserineCombined sources1
Modified residuei272PhosphoserineBy similarity1
Modified residuei305PhosphoserineCombined sources1
Modified residuei307PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6FI81
MaxQBiQ6FI81
PaxDbiQ6FI81
PeptideAtlasiQ6FI81
PRIDEiQ6FI81
TopDownProteomicsiQ6FI81-1 [Q6FI81-1]

PTM databases

iPTMnetiQ6FI81
PhosphoSitePlusiQ6FI81

Expressioni

Tissue specificityi

Ubiquitously expressed. Highly expressed in heart, liver and pancreas.1 Publication

Gene expression databases

BgeeiENSG00000005194
CleanExiHS_CIAPIN1
ExpressionAtlasiQ6FI81 baseline and differential
GenevisibleiQ6FI81 HS

Organism-specific databases

HPAiHPA041350
HPA042182

Interactioni

Subunit structurei

Monomer. Interacts with NDOR1; its oxidized form can be reduced by NDOR1. Interacts with CHCHD4 and may be a substrate for CHCHD4 chaperone activity.2 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi121328, 53 interactors
DIPiDIP-61697N
IntActiQ6FI81, 11 interactors
MINTiQ6FI81
STRINGi9606.ENSP00000377914

Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 4Combined sources3
Beta strandi11 – 16Combined sources6
Helixi22 – 36Combined sources15
Turni37 – 39Combined sources3
Beta strandi40 – 46Combined sources7
Helixi47 – 49Combined sources3
Helixi50 – 53Combined sources4
Beta strandi60 – 66Combined sources7
Beta strandi68 – 70Combined sources3
Helixi77 – 86Combined sources10
Beta strandi87 – 102Combined sources16
Beta strandi105 – 109Combined sources5
Helixi112 – 121Combined sources10
Beta strandi125 – 134Combined sources10
Helixi137 – 147Combined sources11
Beta strandi154 – 162Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LD4NMR-A1-172[»]
2YUINMR-A1-170[»]
4M7RX-ray1.80A/B1-172[»]
ProteinModelPortaliQ6FI81
SMRiQ6FI81
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6FI81

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni6 – 172N-terminal SAM-like domainUniRule annotationAdd BLAST167
Regioni173 – 224LinkerUniRule annotationAdd BLAST52
Regioni225 – 312Intrinsically disorderedUniRule annotationAdd BLAST88
Regioni237 – 251Fe-S binding site AUniRule annotationAdd BLAST15
Regioni274 – 288Fe-S binding site BUniRule annotationAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi274 – 277Cx2C motif 1UniRule annotation4
Motifi285 – 288Cx2C motif 2UniRule annotation4

Domaini

The twin Cx2C motifs are involved in the recognition by the mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.UniRule annotation
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.UniRule annotation
The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters.UniRule annotation2 Publications

Sequence similaritiesi

Belongs to the anamorsin family.UniRule annotation

Phylogenomic databases

eggNOGiKOG4020 Eukaryota
COG5636 LUCA
GeneTreeiENSGT00390000011417
HOGENOMiHOG000241118
HOVERGENiHBG051104
InParanoidiQ6FI81
OMAiQFVAVVW
OrthoDBiEOG091G0OTI
PhylomeDBiQ6FI81
TreeFamiTF314449

Family and domain databases

HAMAPiMF_03115 Anamorsin, 1 hit
InterProiView protein in InterPro
IPR007785 Anamorsin
IPR013216 Methyltransf_11
IPR029063 SAM-dependent_MTases
PANTHERiPTHR13273 PTHR13273, 1 hit
PfamiView protein in Pfam
PF05093 CIAPIN1, 2 hits
PF08241 Methyltransf_11, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6FI81-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADFGISAGQ FVAVVWDKSS PVEALKGLVD KLQALTGNEG RVSVENIKQL
60 70 80 90 100
LQSAHKESSF DIILSGLVPG STTLHSAEIL AEIARILRPG GCLFLKEPVE
110 120 130 140 150
TAVDNNSKVK TASKLCSALT LSGLVEVKEL QREPLTPEEV QSVREHLGHE
160 170 180 190 200
SDNLLFVQIT GKKPNFEVGS SRQLKLSITK KSSPSVKPAV DPAAAKLWTL
210 220 230 240 250
SANDMEDDSM DLIDSDELLD PEDLKKPDPA SLRAASCGEG KKRKACKNCT
260 270 280 290 300
CGLAEELEKE KSREQMSSQP KSACGNCYLG DAFRCASCPY LGMPAFKPGE
310
KVLLSDSNLH DA
Length:312
Mass (Da):33,582
Last modified:January 4, 2005 - v2
Checksum:i70A71D44074ABFBA
GO
Isoform 2 (identifier: Q6FI81-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.

Note: No experimental confirmation available.
Show »
Length:108
Mass (Da):11,735
Checksum:iC9B53F80FA24398A
GO
Isoform 3 (identifier: Q6FI81-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-66: SAHKESSFDIILSG → C

Show »
Length:299
Mass (Da):32,213
Checksum:i29CA61B57C265FE7
GO

Sequence cautioni

The sequence AAC24312 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti142S → F in CAB66548 (PubMed:11230166).Curated1
Sequence conflicti142S → F in CAG38576 (Ref. 4) Curated1
Sequence conflicti278Y → C in CAG38576 (Ref. 4) Curated1
Sequence conflicti289P → T in CAB66548 (PubMed:11230166).Curated1
Sequence conflicti289P → T in CAG38576 (Ref. 4) Curated1
Sequence conflicti310H → N in CAB66548 (PubMed:11230166).Curated1
Sequence conflicti310H → N in CAG38576 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03374734A → E. Corresponds to variant dbSNP:rs11557672Ensembl.1
Natural variantiVAR_03374852Q → E. Corresponds to variant dbSNP:rs11557674Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0123601 – 204Missing in isoform 2. 1 PublicationAdd BLAST204
Alternative sequenceiVSP_01236153 – 66SAHKE…IILSG → C in isoform 3. 3 PublicationsAdd BLAST14

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF248964 mRNA Translation: AAG44562.1
AL136613 mRNA Translation: CAB66548.1
AF116609 mRNA Translation: AAF71034.1
CR533545 mRNA Translation: CAG38576.1
AK292281 mRNA Translation: BAF84970.1
AC004382 Genomic DNA Translation: AAC24311.1
AC004382 Genomic DNA Translation: AAC24312.1 Sequence problems.
CH471092 Genomic DNA Translation: EAW82923.1
BC002568 mRNA Translation: AAH02568.1
BC024196 mRNA Translation: AAH24196.1
BC067303 mRNA Translation: AAH67303.1
BC071740 mRNA Translation: AAH71740.1
CCDSiCCDS10781.2 [Q6FI81-1]
CCDS76876.1 [Q6FI81-3]
RefSeqiNP_001295276.1, NM_001308347.1 [Q6FI81-3]
NP_001295287.1, NM_001308358.1
NP_064709.2, NM_020313.3 [Q6FI81-1]
UniGeneiHs.4900

Genome annotation databases

EnsembliENST00000394391; ENSP00000377914; ENSG00000005194 [Q6FI81-1]
ENST00000567518; ENSP00000456114; ENSG00000005194 [Q6FI81-3]
GeneIDi57019
KEGGihsa:57019
UCSCiuc002ell.2 human [Q6FI81-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiCPIN1_HUMAN
AccessioniPrimary (citable) accession number: Q6FI81
Secondary accession number(s): A8K8B6
, O75206, O75207, Q9H0W1, Q9P1L7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: April 25, 2018
This is version 132 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health